ID   QTRT2_CAEEL             Reviewed;         373 AA.
AC   Q9NEU3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Queuine tRNA-ribosyltransferase accessory subunit 2 {ECO:0000255|HAMAP-Rule:MF_03043};
DE   AltName: Full=Queuine tRNA-ribosyltransferase domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03043};
GN   Name=tgt-2 {ECO:0000255|HAMAP-Rule:MF_03043}; ORFNames=Y39B6A.35;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Non-catalytic subunit of the queuine tRNA-ribosyltransferase
CC       (TGT) that catalyzes the base-exchange of a guanine (G) residue with
CC       queuine (Q) at position 34 (anticodon wobble position) in tRNAs with
CC       GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the
CC       hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
CC       cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). {ECO:0000255|HAMAP-
CC       Rule:MF_03043}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03043};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03043};
CC   -!- SUBUNIT: Heterodimer of a catalytic subunit and an accessory subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_03043}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03043}.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       QTRT2 subfamily. {ECO:0000255|HAMAP-Rule:MF_03043}.
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DR   EMBL; AL132948; CAC51046.1; -; Genomic_DNA.
DR   PIR; T45043; T45043.
DR   RefSeq; NP_741662.1; NM_171572.3.
DR   AlphaFoldDB; Q9NEU3; -.
DR   SMR; Q9NEU3; -.
DR   STRING; 6239.Y39B6A.35; -.
DR   EPD; Q9NEU3; -.
DR   PaxDb; Q9NEU3; -.
DR   PeptideAtlas; Q9NEU3; -.
DR   EnsemblMetazoa; Y39B6A.35.1; Y39B6A.35.1; WBGene00006567.
DR   GeneID; 180244; -.
DR   KEGG; cel:CELE_Y39B6A.35; -.
DR   UCSC; Y39B6A.35; c. elegans.
DR   CTD; 180244; -.
DR   WormBase; Y39B6A.35; CE21692; WBGene00006567; tgt-2.
DR   eggNOG; KOG3909; Eukaryota.
DR   GeneTree; ENSGT00530000063679; -.
DR   HOGENOM; CLU_037350_0_0_1; -.
DR   InParanoid; Q9NEU3; -.
DR   OMA; AKEMTAW; -.
DR   OrthoDB; 883398at2759; -.
DR   PhylomeDB; Q9NEU3; -.
DR   PRO; PR:Q9NEU3; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00006567; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0101030; P:tRNA-guanine transglycosylation; IBA:GO_Central.
DR   Gene3D; 3.20.20.105; -; 1.
DR   HAMAP; MF_03043; QTRT2; 1.
DR   InterPro; IPR028592; QTRTD1.
DR   InterPro; IPR036511; TGT-like_sf.
DR   InterPro; IPR002616; tRNA_ribo_trans-like.
DR   Pfam; PF01702; TGT; 1.
DR   SUPFAM; SSF51713; SSF51713; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..373
FT                   /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT                   /id="PRO_0000383929"
FT   BINDING         320
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         322
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         325
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         351
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ   SEQUENCE   373 AA;  41913 MW;  349766C1C67ED4E2 CRC64;
     MVKFQIEKKT LLGRLGKIDT WGSVEVNHQT PSFQTYLRAG HIPHLTWEVA ENQLKLEQTH
     IFQMTLPTLV SNAKIIEKFG KGAAKFCGMP AGAAVHLTPF DPLGKLPGGY NDSKSVAIWT
     ANGKVSLDVK MWREIINSFG CGSIETLVDY DTPKDVGQKK LVKAVDRTKT FQEQLFQQDE
     KVNGERIVSL GGGFSKYHRR KCAVDVGLAE NIAGYTVEFR EFTEGKETDD KEMKELLEET
     FSPLPPTKLR CISGPFNPKT VLFLVQQGID LFDSSFPVKL AEEGHAFCLS DDFPTSSKYE
     VVDFNNEKFA DDFTALFDGC ACYTCTKYTK GYLQHLLNTR ELLASILLVI HNMTEYDKMF
     KLIRSSLENS EGL